MULTISPECIES: malate dehydrogenase [Shigella].

LOCUS       WP_005050705             312 aa            linear   BCT 17-NOV-2023
ACCESSION   WP_005050705
VERSION     WP_005050705.1
KEYWORDS    RefSeq.
SOURCE      Shigella
  ORGANISM  Shigella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 312)
  AUTHORS   Hannenhalli,S.S. and Russell,R.B.
  TITLE     Analysis and prediction of functional sub-types from protein
            sequence alignments
  JOURNAL   J Mol Biol 303 (1), 61-76 (2000)
   PUBMED   11021970
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01772.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..312
                     /organism="Shigella"
                     /db_xref="taxon:620"
     gene            1..312
                     /gene="mdh"
     Protein         1..312
                     /product="malate dehydrogenase"
                     /EC_number="1.1.1.37"
                     /GO_function="GO:0030060 - L-malate dehydrogenase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006099 - tricarboxylic acid cycle
                     [Evidence IEA]"
                     /calculated_mol_wt=32218
     Region          1..310
                     /region_name="MDH_glyoxysomal_mitochondrial"
                     /note="Glyoxysomal and mitochondrial malate
                     dehydrogenases; cd01337"
                     /db_xref="CDD:133422"
     Site            order(9..12,34,76,78..79,90,94,97,117,119,146,149,177,223,
                     227)
                     /site_type="other"
                     /note="NAD binding site [chemical binding]"
                     /db_xref="CDD:133422"
     Site            order(14,44..45,47..49,152..153,156,209,212,216..217,
                     223..226,229)
                     /site_type="other"
                     /note="dimerization interface [polypeptide binding]"
                     /db_xref="CDD:133422"
     Site            order(81,87,119,153,177,210)
                     /site_type="other"
                     /note="Substrate binding site [chemical binding]"
                     /db_xref="CDD:133422"
ORIGIN      
        1 mkvavlgaag gigqalalll ktqlpsgsel slydiapvtp gvavdlship tavkikgfsg
       61 edatpalega dvvlisagva rkpgmdrsdl fnvnagivkn lvqqvakncp kacigiitnp
      121 vnttvaiaae vlkkagvydk nklfgvttld iirsntfvae lkgkqpgeve vpvigghsgv
      181 tilpllsqvp gvsfteqeva dltkriqnag tevveakagg gsatlsmgqa aarfglslvr
      241 alqgeqgvve cayvegdgqy arffsqplll gkngveerks igtlsafeqn alegmldtlk
      301 kdialgkefv nk